Kinetics of interactions between apomyoglobin and phospholipid membrane

Balobanov, Vitaly A.; Ilina, Nelly; Katina, N. S.; Kashparov, I. A.; Долгих, Д. А.; Bychkova, Valentina E.

doi:10.1134/s0026893310040187

Cited by 3 publications

(3 citation statements)

References 37 publications

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“…On the other hand, native apoMb in the presence of the same membranes loses its N structure and transforms into an analogous state similar to the MG (Fig. 4) [65]. Analysis of the kinetics of interaction of native apoMb with the surface of vesicles demonstrated that when the content of negatively charged PhL drops from 100 to 20%, the interaction remains practically the same.…”

Section: Conformational State Of Globular Proteins In the Presence Ofmentioning

confidence: 90%

“…The binding effi ciency decreases with decreasing concentration of PG in mixed vesicles. At the same time, the rate of mem brane-protein interaction slows, and the stability of the protein structure has a noticeable effect as well [65]. Additionally, POPG -SUV can unfold native apoMb and fold the protein unfolded by urea.…”

Section: Effect Of Different Types Of Phospholipid Membranes On Protementioning

confidence: 99%

“…Effect of protein stability on protein interactions with phospholipid membranes (adapted from[65]). a) Changes in Trp fluorescence spectra upon addition of apoMb in the N and urea unfolded U states to a solution of mixed vesicles (POPG-POPC) at 20% negatively charged POPG.…”

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confidence: 99%

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How membrane surface affects protein structure

Bychkova

Basova

Balobanov

2014

Biochemistry Moscow

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The immediate environment of the negatively charged membrane surface is characterized by decreased dielectric constant and pH value. These conditions can be modeled by water-alcohol mixtures at moderately low pH. Several globular proteins were investigated under these conditions, and their conformational behavior in the presence of phospholipid membranes was determined, as well as under conditions modeling the immediate environment of the membrane surface. These proteins underwent conformational transitions from the native to a molten globule-like state. Increased flexibility of the protein structure facilitated protein functioning. Our experimental data allow understanding forces that affect the structure of a protein functioning near the membrane surface (in other words, in the membrane field). Similar conformational states are widely reported in the literature. This indicates that the negatively charged membrane surface can serve as a moderately denaturing agent in the cell. We conclude that the effect of the membrane field on the protein structure must be taken into account.

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Section: Conformational State Of Globular Proteins In the Presence Ofmentioning

confidence: 90%

Section: Effect Of Different Types Of Phospholipid Membranes On Protementioning

confidence: 99%

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How membrane surface affects protein structure

Bychkova

Basova

Balobanov

2014

Biochemistry Moscow

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Membrane-induced changes in the holomyoglobin tertiary structure: interplay with function

et al. 2014

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The effect of anionic phospholipid membranes on holomyoglobin (holoMb) conformation and deoxygenation was studied. HoloMb structural changes and behavior in the presence of membranes were monitored by a variety of techniques including far UV and near UV circular dichroism, tryptophan (Trp) fluorescence, absorbance in the Soret region, differential scanning calorimetry, (1)H-NMR spectroscopy, size exclusion chromatography, and macroscopic diffusion. Kinetics of deoxygenation was monitored by absorption at 581 nm. The results gave evidence that proximity to a negatively charged membrane surface can cause destabilization of the structure of holomyoglobin, which delivers oxygen (O2) to mitochondria. It was shown that holoMb undergoes the native-to-intermediate-state transition in the presence of anionic phospholipid membranes at neutral pH, and that in this state it is able to interact with the membranes. When in the intermediate state, holoMb loses its rigid tertiary structure but preserves a pronounced secondary one. The presence of anionic phospholipid membranes substantially accelerates the process of deoxygenation. A possible functional role of the more flexible protein structure acquired in immediate proximity to the membrane surface is discussed.

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